5O7Z

Crystal Structure of R67A Mutant of alpha-L-arabinofuranosidase Ara51 from Clostridium thermocellum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000272	biological_process	polysaccharide catabolic process
A	0005737	cellular_component	cytoplasm
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0031222	biological_process	arabinan catabolic process
A	0046373	biological_process	L-arabinose metabolic process
A	0046556	molecular_function	alpha-L-arabinofuranosidase activity
B	0000272	biological_process	polysaccharide catabolic process
B	0005737	cellular_component	cytoplasm
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0031222	biological_process	arabinan catabolic process
B	0046373	biological_process	L-arabinose metabolic process
B	0046556	molecular_function	alpha-L-arabinofuranosidase activity
C	0000272	biological_process	polysaccharide catabolic process
C	0005737	cellular_component	cytoplasm
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0031222	biological_process	arabinan catabolic process
C	0046373	biological_process	L-arabinose metabolic process
C	0046556	molecular_function	alpha-L-arabinofuranosidase activity
D	0000272	biological_process	polysaccharide catabolic process
D	0005737	cellular_component	cytoplasm
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0031222	biological_process	arabinan catabolic process
D	0046373	biological_process	L-arabinose metabolic process
D	0046556	molecular_function	alpha-L-arabinofuranosidase activity
E	0000272	biological_process	polysaccharide catabolic process
E	0005737	cellular_component	cytoplasm
E	0016787	molecular_function	hydrolase activity
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0031222	biological_process	arabinan catabolic process
E	0046373	biological_process	L-arabinose metabolic process
E	0046556	molecular_function	alpha-L-arabinofuranosidase activity
F	0000272	biological_process	polysaccharide catabolic process
F	0005737	cellular_component	cytoplasm
F	0016787	molecular_function	hydrolase activity
F	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
F	0031222	biological_process	arabinan catabolic process
F	0046373	biological_process	L-arabinose metabolic process
F	0046556	molecular_function	alpha-L-arabinofuranosidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue DIO C 601

Chain	Residue
C	PHE25
C	GLU27
C	TRP97
C	TYR244
C	GLU292
C	LEU319
C	GLN352

---

site_id	AC2
Number of Residues	6
Details	binding site for residue DIO D 601

Chain	Residue
D	TYR244
D	GLU292
D	TRP296
D	GLN352
D	PHE25
D	GLU27

---

site_id	AC3
Number of Residues	7
Details	binding site for residue DIO E 601

Chain	Residue
E	GLU27
E	GLY71
E	ASN72
E	TRP97
E	GLU173
E	TYR244
E	GLU292

---

site_id	AC4
Number of Residues	9
Details	binding site for residue DIO F 601

Chain	Residue
F	GLU27
F	GLY71
F	ASN72
F	TRP97
F	GLU173
F	TYR244
F	GLU292
F	TRP296
F	GLN352

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"16336192","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16336192","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2017","submissionDatabase":"PDB data bank","authors":["Pennec A.","Lafite P.","Ferrieres V.","Daniellou R."]}},{"source":"PubMed","id":"16336192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2C7F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2C8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5O80","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5O82","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2017","submissionDatabase":"PDB data bank","authors":["Pennec A.","Lafite P.","Ferrieres V.","Daniellou R."]}},{"source":"PubMed","id":"16336192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2C7F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5O82","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2017","submissionDatabase":"PDB data bank","authors":["Pennec A.","Lafite P.","Ferrieres V.","Daniellou R."]}},{"source":"PubMed","id":"16336192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2C8N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5O80","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	12
Details	Site: {"description":"Important for substrate recognition","evidences":[{"source":"UniProtKB","id":"Q9XBQ3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---